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The process of amino acid building to create protein in translation is a subject of various physic models for a long time starting from the first detailed kinetic models such as [24] or others taking into account stochastic aspects of translation and using computer simulations. Many chemical kinetics-based models of protein synthesis have been ...
Translation is one of the key energy consumers in cells, hence it is strictly regulated. Numerous mechanisms have evolved that control and regulate translation in eukaryotes as well as prokaryotes. Regulation of translation can impact the global rate of protein synthesis which is closely coupled to the metabolic and proliferative state of a cell.
Protein synthesis is a very similar process for both prokaryotes and eukaryotes but there are some distinct differences. [1] Protein synthesis can be divided broadly into two phases: transcription and translation. During transcription, a section of DNA encoding a protein, known as a gene, is converted into a molecule called messenger RNA (mRNA).
Phosphorylation is highly effective for controlling the enzyme activity and is the most common change after translation. [ 2 ] Many eukaryotic and prokaryotic proteins also have carbohydrate molecules attached to them in a process called glycosylation , which can promote protein folding and improve stability as well as serving regulatory functions.
In virology, the term transcription is used when referring to mRNA synthesis from a viral RNA molecule. The genome of many RNA viruses [a] is composed of negative-sense RNA which acts as a template for positive sense viral messenger RNA - a necessary step in the synthesis of viral proteins needed for viral replication.
Once translation initiation is complete, the first aminoacyl tRNA is located in the P/P site, ready for the elongation cycle described below. During translation elongation, tRNA first binds to the ribosome as part of a complex with elongation factor Tu or its eukaryotic or archaeal counterpart. This initial tRNA binding site is called the A/T site.
Recent experiments have reported that protein translation can also initiate from the A-site. Using toeprinting assay, it has been shown that protein synthesis initiates from the A-site of the ribosome (eukaryotic) in the cricket paralysis virus (CrPV). IGR-IRES (intragenic regions-internal ribosome entry sites) can assemble 80S ribosomes from ...
Initiation of translation in bacteria involves the assembly of the components of the translation system, which are: the two ribosomal subunits (50S and 30S subunits); the mature mRNA to be translated; the tRNA charged with N-formylmethionine (the first amino acid in the nascent peptide); guanosine triphosphate (GTP) as a source of energy, and the three prokaryotic initiation factors IF1, IF2 ...